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Purification of bacteriall-methionine γ-lyase

Authors
Journal
Analytical Biochemistry
0003-2697
Publisher
Elsevier
Publication Date
Volume
138
Issue
2
Identifiers
DOI: 10.1016/0003-2697(84)90832-7
Keywords
  • Methionine γ-Lyase
  • Bacterial Enzyme
  • Enzyme Purification
  • Vitamin B6Enzyme
  • Sulfur Amino Acids
Disciplines
  • Biology

Abstract

Abstract A rapid procedure for the purification of l-methionine γ-lyase from Pseudomonas putida ICR 3460 by DEAE-TOYOPEARL 650M and DEAE-Sephadex A-50 column chromatography is presented. The enzyme was purified with an average yield of 75% and showed about 10-fold higher specific activity than the enzyme from P. putida (= P. ovalis) IFO 3738 reported previously ( H. Tanaka, N. Esaki, and K. Soda (1976) FEBS Lett. 66, 307–311). The present enzyme has a molecular weight of about 172,000 and consists of four subunits with identical molecular weights (43,000). It shows the typical absorption spectrum of pyridoxal enzyme with maxima at 278 and 420 nm, and contains 4 mol of pyridoxal 5′-phosphate per mole of enzyme. The enzyme has a multicatalytic function similar to the enzyme of P. putida IFO 3738 ( K. Soda, H. Tanaka, and N. Esaki (1983) Trends Biochem. Sci. 8, 214–217).

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